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Conserved domains on  [gi|447040780|ref|WP_001118036|]
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MULTISPECIES: 2-oxoglutaramate amidase [Enterobacteriaceae]

Protein Classification

nitrilase family protein( domain architecture ID 10013522)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


:

Pssm-ID: 182461  Cd Length: 256  Bit Score: 560.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTSGFAMEAAASSLAQDDVVNWMTAKAQQCNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  81 VALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 161 YVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 447040780 241 REKFPAWQDADEFRLW 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 560.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTSGFAMEAAASSLAQDDVVNWMTAKAQQCNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  81 VALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 161 YVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 447040780 241 REKFPAWQDADEFRLW 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-253 1.09e-153

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 427.73  E-value: 1.09e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTSGFAMEAAAssLAQD---DVVNWMTAKAQQCNALIAG 79
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEA--LAEPmngPTLQWMKAQAKKKGAAITG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  80 SVALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLA 159
Cdd:cd07575   79 SLIIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 160 LYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIdAELSMAALRE 239
Cdd:cd07575  159 LYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQE 237

                        250
                 ....*....|....
gi 447040780 240 YREKFPAWQDADEF 253
Cdd:cd07575  238 FREKFPFLKDADSF 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-253 1.30e-72

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 222.82  E-value: 1.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQPLVWMDGPANLRHFDRQLEGITGR--DVIVLPEMFTSGFAMEAAASSLAQDDV----VNWMTAKAQQCNALI 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  78 AGSVALQTESGSV-NRFLLVEPGGT-VHFYDKRHLFRM--ADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNL 153
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 154 --NDYDLALYVANWPAPRSL-HWQALLTARAIENQAYVAGCNRVGSDGnGCHYRGDSRVINPQGEIIATADAHQATRIdA 230
Cdd:COG0388  162 alAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEEGLLV-A 239

                        250       260
                 ....*....|....*....|...
gi 447040780 231 ELSMAALREYREKFPAWQDADEF 253
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPD 262
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-241 1.11e-31

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 117.07  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780    5 KITLLQQPLVWMDGPANLRHFDRQLEGITGR--DVIVLPEMFTSGFAMEAAASSLAQD---DVVNWMTAKAQQCN-ALIA 78
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAHFLEAAEVgdgETLAGLAALARKNGiAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   79 GSVALQTESGSV-NRFLLVEPGGTVHF-YDKRHLFRMAD-----EHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRLyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  152 --NLNDYDLALYVAN----WPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240

                         250
                  ....*....|....*.
gi 447040780  226 TRIDAELSMAALREYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 6.78e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 72.24  E-value: 6.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 105 YDKRHL---FRMaDEHLHYKAGNA-RVIVEWRGWRILPLVCYDLRFPVWSRNL--NDYDLALYVANW---PApRSLHWQA 175
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARRLalDGADVLVLPAAWvrgPL-KEHHWET 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447040780 176 LLTARAIENQAYVAGcnrVGSDGNgchyR--GDSRVINPQGEIIATAdAHQATRIDAELSMAALREYREKFP 245
Cdd:NF033621 185 LLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 560.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTSGFAMEAAASSLAQDDVVNWMTAKAQQCNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  81 VALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 161 YVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 447040780 241 REKFPAWQDADEFRLW 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-253 1.09e-153

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 427.73  E-value: 1.09e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTSGFAMEAAAssLAQD---DVVNWMTAKAQQCNALIAG 79
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEA--LAEPmngPTLQWMKAQAKKKGAAITG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  80 SVALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLA 159
Cdd:cd07575   79 SLIIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 160 LYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIdAELSMAALRE 239
Cdd:cd07575  159 LYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQE 237

                        250
                 ....*....|....
gi 447040780 240 YREKFPAWQDADEF 253
Cdd:cd07575  238 FREKFPFLKDADSF 251
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-249 9.95e-77

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143607  Cd Length: 253  Bit Score: 232.81  E-value: 9.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   5 KITLLQQPLVWMDGPANLRHFDRQLEGI--TGRDVIVLPEMFTSGFAME--AAASSLAQDDVVNWMTAKAQQCNA-LIAG 79
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAaaAGADLIVLPEMWNTGYFLDdlYELADEDGGETVSFLSELAKKHGVnIVAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  80 SVALQTESGSVNRFLLVEPGGT-VHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNL--NDY 156
Cdd:cd07583   81 SVAEKEGGKLYNTAYVIDPDGElIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLalEGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 157 DLALYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGcHYRGDSRVINPQGEIIATADAHQATrIDAELSMAA 236
Cdd:cd07583  161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGN-EFGGHSMVIDPWGEVLAEAGEEEEI-LTAEIDLEE 238

                        250
                 ....*....|...
gi 447040780 237 LREYREKFPAWQD 249
Cdd:cd07583  239 VAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-253 1.30e-72

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 222.82  E-value: 1.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQPLVWMDGPANLRHFDRQLEGITGR--DVIVLPEMFTSGFAMEAAASSLAQDDV----VNWMTAKAQQCNALI 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  78 AGSVALQTESGSV-NRFLLVEPGGT-VHFYDKRHLFRM--ADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNL 153
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 154 --NDYDLALYVANWPAPRSL-HWQALLTARAIENQAYVAGCNRVGSDGnGCHYRGDSRVINPQGEIIATADAHQATRIdA 230
Cdd:COG0388  162 alAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEEGLLV-A 239

                        250       260
                 ....*....|....*....|...
gi 447040780 231 ELSMAALREYREKFPAWQDADEF 253
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPD 262
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 6-249 7.54e-59

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 187.15  E-value: 7.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   6 ITLLQQPLVWMDGPANLRHFDRQLE--GITGRDVIVLPEMFTSG--FAMEAAASSLAQDD---VVNWMTAKAQQCNALIA 78
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKeaAEQGADLIVLPELFLTGysFESAKEDLDLAEELdgpTLEALAELAKELGIYIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  79 GSVALQTESGSVNRFLLVEPGGT-VHFYDKRHLFRMaDEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNL--ND 155
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDPDGEiIGKYRKIHLFDF-GERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARELalKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 156 YDLALYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYrGDSRVINPQGEIIATADAHQATRIdAELSMA 235
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFA-GGSMIVDPDGEVLAEASEEEGILV-AELDLD 237

                        250
                 ....*....|....
gi 447040780 236 ALREYREKFPAWQD 249
Cdd:cd07197  238 ELREARKRWSYLRD 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 20-248 8.99e-37

Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10.


Pssm-ID: 143596  Cd Length: 265  Bit Score: 130.62  E-value: 8.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  20 ANLRHFDRQLE--GITGRDVIVLPEMFTS----GFAMEAAASSLAQDDVVNWMTAKAQQCN-ALIAGSVALQTESGS--V 90
Cdd:cd07572   15 ANLARAKELIEeaAAQGAKLVVLPECFNYpggtDAFKLALAEEEGDGPTLQALSELAKEHGiWLVGGSIPERDDDDGkvY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  91 NRFLLVEPGGT-VHFYDKRHLF-------RMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDY--DLAL 160
Cdd:cd07572   95 NTSLVFDPDGElVARYRKIHLFdvdvpggISYRESDTLTPGDEVVVVDTPFGKIGLGICYDLRFPELARALARQgaDILT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 161 YvanwPA-------PrsLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATrIDAELS 233
Cdd:cd07572  175 V----PAaftmttgP--AHWELLLRARAIENQCYVVAAAQAGDHEAGRETYGHSMIVDPWGEVLAEAGEGEGV-VVAEID 247

                        250
                 ....*....|....*
gi 447040780 234 MAALREYREKFPAWQ 248
Cdd:cd07572  248 LDRLEEVRRQIPVLK 262
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 5-249 5.90e-36

Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 128.08  E-value: 5.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   5 KITLLQQPLVWMDGPANLRHFDRQLEGITGR--DVIVLPEMFTSGFAMEAAASSLAQ---DDVVNWMTAKAQQCNALIAG 79
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAgaDLLVFPELFLTGYNIGDAVARLAEpadGPALQALRAIARRHGIAIVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  80 SVALQTESGSVNRFLLVEPGGTV-HFYDKRHLFRmADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRnlndyDL 158
Cdd:cd07576   81 GYPERAGGAVYNAAVLIDEDGTVlANYRKTHLFG-DSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVR-----AL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 159 ALYVANW---PAPRSLHW----QALLTARAIENQAYVAGCNRVGSDGNGChYRGDSRVINPQGEIIATADAHqATRIDAE 231
Cdd:cd07576  155 ALAGADLvlvPTALMEPYgfvaRTLVPARAFENQIFVAYANRCGAEDGLT-YVGLSSIAGPDGTVLARAGRG-EALLVAD 232

                        250
                 ....*....|....*...
gi 447040780 232 LSMAALREYREKFPAWQD 249
Cdd:cd07576  233 LDPAALAAARRENPYLAD 250
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-241 1.11e-31

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 117.07  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780    5 KITLLQQPLVWMDGPANLRHFDRQLEGITGR--DVIVLPEMFTSGFAMEAAASSLAQD---DVVNWMTAKAQQCN-ALIA 78
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAHFLEAAEVgdgETLAGLAALARKNGiAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   79 GSVALQTESGSV-NRFLLVEPGGTVHF-YDKRHLFRMAD-----EHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRLyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  152 --NLNDYDLALYVAN----WPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240

                         250
                  ....*....|....*.
gi 447040780  226 TRIDAELSMAALREYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 36-243 8.28e-28

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 107.00  E-value: 8.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  36 DVIVLPEMFTSGFA------MEAAASSLAQDDVVNWMTAKAQQCNALIAGSVALQTESGSVNRFLLVEPGGTVHFYDKRH 109
Cdd:cd07577   31 DLIVLPELFNTGYAftskeeVASLAESIPDGPTTRFLQELARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIYRKTH 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 110 LFRmaDEHLHYKAGN-ARVIVEWRGWRILPLVCYDLRFPVWSRN--LNDYDLALYVANWPAPrslHWQALLTARAIENQA 186
Cdd:cd07577  111 LFY--EEKLFFEPGDtGFRVFDIGDIRIGVMICFDWYFPEAARTlaLKGADIIAHPANLVLP---YCPKAMPIRALENRV 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 187 YVAGCNRVGSDGNGC---HYRGDSRVINPQGEIIATADAHQATRIDAELSmaaLREYREK 243
Cdd:cd07577  186 FTITANRIGTEERGGetlRFIGKSQITSPKGEVLARAPEDGEEVLVAEID---PRLARDK 242
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 16-245 2.83e-27

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143605  Cd Length: 255  Bit Score: 105.35  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  16 MDGPANLRHFDRQLEGITGR--DVIVLPE--MFTSGF---AMEAAASSLaQDDVVNWMTAKAQQCNALIAGSVALQTESG 88
Cdd:cd07581   10 GDKEENLEKVRRLLAEAAAAgaDLVVFPEytMARFGDgldDYARVAEPL-DGPFVSALARLARELGITVVAGMFEPAGDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  89 SV-NRFLLVEPGGTVH-FYDKRHLFrmaD-----EHLHYKAGN--ARVIVEWRGWRILPLVCYDLRFPVWSRNLNDY--D 157
Cdd:cd07581   89 RVyNTLVVVGPDGEIIaVYRKIHLY---DafgfrESDTVAPGDelPPVVFVVGGVKVGLATCYDLRFPELARALALAgaD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 158 LALYVANW-PAPRSL-HWQALLTARAIENQAYVAGCNRVGSdgngcHYRGDSRVINPQGEIIATADAHQATRIdAELSMA 235
Cdd:cd07581  166 VIVVPAAWvAGPGKEeHWETLLRARALENTVYVAAAGQAGP-----RGIGRSMVVDPLGVVLADLGEREGLLV-ADIDPE 239

                        250
                 ....*....|
gi 447040780 236 ALREYREKFP 245
Cdd:cd07581  240 RVEEAREALP 249
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-249 2.96e-25

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143608  Cd Length: 258  Bit Score: 100.14  E-value: 2.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   5 KITLLQQPLVWMDGPANLR---HFDRQLeGITGRDVIVLPEMFTSGFAME------AAASSLAQDDVVNWMTAKAQQCNA 75
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKkaaELCKEA-AAEGADLICFPELATTGYRPDllgpklWELSEPIDGPTVRLFSELAKELGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  76 -LIAGSVALQTESGSV-NRFLLVEPGG-TVHFYDKRHLFrmADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSR- 151
Cdd:cd07584   80 yIVCGFVEKGGVPGKVyNSAVVIDPEGeSLGVYRKIHLW--GLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVARi 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 152 -NLNDYDLALYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNgCHYRGDSRVINPQGEIIATADAHQATRIDA 230
Cdd:cd07584  158 lTLKGAEVIFCPSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGD-LVLFGKSKILNPRGQVLAEASEEAEEILYA 236

                        250
                 ....*....|....*....
gi 447040780 231 ELSMAALREYREKFPAWQD 249
Cdd:cd07584  237 EIDLDAIADYRMTLPYLKD 255
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 4-251 1.32e-22

Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143598  Cd Length: 280  Bit Score: 93.42  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQPlvwMDGPANLRHFDRQLEGI------TGRDVIVLPEMFT---SGFAMEAAASSLAQ--------DDVVNWM 66
Cdd:cd07574    1 VRVAAAQYP---LRRYASFEEFAAKVEYWvaeaagYGADLLVFPEYFTmelLSLLPEAIDGLDEAiralaaltPDYVALF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  67 TAKAQQCNA-LIAGSVALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLR 145
Cdd:cd07574   78 SELARKYGInIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 146 FPVWSRNLNDY--DLaLYVANWPAPRSLHWQALLT--ARAIENQAYVAGCNRVGS-------DGNgchyRGDSRVINP-- 212
Cdd:cd07574  158 FPELARALAEAgaDL-LLVPSCTDTRAGYWRVRIGaqARALENQCYVVQSGTVGNapwspavDVN----YGQAAVYTPcd 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 447040780 213 -----QGeIIATADAHQATRIDAELSMAALREYREKFPAWQDAD 251
Cdd:cd07574  233 fgfpeDG-ILAEGEPNTEGWLIADLDLEALRRLREEGSVRNLRD 275
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 26-218 4.96e-20

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 86.22  E-value: 4.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  26 DRQLEGIT---------GRDVIVLPEMFTSGF----AMEAAASSLAQDDVVNWMTAKAQQCNALIAGSVAlQTESGSVNR 92
Cdd:cd07585   15 ARNLAVIArwtrkaaaqGAELVCFPEMCITGYthvrALSREAEVPDGPSTQALSDLARRYGLTILAGLIE-KAGDRPYNT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  93 FLLVEPGGTVHFYDKRHLFRMadEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLN----DYDLALYVA--NWP 166
Cdd:cd07585   94 YLVCLPDGLVHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRATAllgaEILFAPHATpgTTS 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447040780 167 APRSLHWQALLTARAIENQAYVAGCNRVGSDGnGCHYRGDSRVINPQGEIIA 218
Cdd:cd07585  172 PKGREWWMRWLPARAYDNGVFVAACNGVGRDG-GEVFPGGAMILDPYGRVLA 222
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 20-251 8.05e-20

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 85.80  E-value: 8.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  20 ANL-RHFDRQLEGI-TGRDVIVLPEMFTSGFAMEAAASSLAqddvvnwMTAKAQQCNALIAGSVALQTESGSV------- 90
Cdd:cd07586   16 ENLeKHLEIIETAReRGADLVVFPELSLTGYNLGDLVYEVA-------MHADDPRLQALAEASGGICVVFGFVeegrdgr 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  91 --NRFLLVEPGGTVHFYDKRHL--FRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFP--VWSRNLNDYDLALYVAN 164
Cdd:cd07586   89 fyNSAAYLEDGRVVHVHRKVYLptYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPslPYLLALDGADVIFIPAN 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 165 WPAPRSLH-------WQALLTARAIENQAYVAGCNRVGSDGnGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAAL 237
Cdd:cd07586  169 SPARGVGGdfdneenWETLLKFYAMMNGVYVVFANRVGVED-GVYFWGGSRVVDPDGEVVAEAPLFEEDLLVAELDRSAI 247

                        250
                 ....*....|....
gi 447040780 238 REYREKFPAWQDAD 251
Cdd:cd07586  248 RRARFFSPTFRDED 261
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 20-241 3.95e-18

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143604  Cd Length: 268  Bit Score: 81.24  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  20 ANLRHFDRQLEGI--TGRDVIVLPEMFTSG--FAMEAAASSLAQD-----DVVNWmTAKAQQCNALIAGSVALQTESGSV 90
Cdd:cd07580   16 ANLARSIELIREAadAGANLVVLPELANTGyvFESRDEAFALAEEvpdgaSTRAW-AELAAELGLYIVAGFAERDGDRLY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  91 NRFLLVEPGGTVHFYDKRHLFrmADEHLHYKAGNARV-IVEWRGWRILPLVCYDLRFPVWSRN--LNDYDLALYVANW-P 166
Cdd:cd07580   95 NSAVLVGPDGVIGTYRKAHLW--NEEKLLFEPGDLGLpVFDTPFGRIGVAICYDGWFPETFRLlaLQGADIVCVPTNWvP 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 167 APRSLHWQA-----LLTARAIENQAYVAGCNRVGSDgNGCHYRGDSRVINPQGEIIAT-ADAHQATRIDAELSMAALREY 240
Cdd:cd07580  173 MPRPPEGGPpmaniLAMAAAHSNGLFIACADRVGTE-RGQPFIGQSLIVGPDGWPLAGpASGDEEEILLADIDLTAARRK 251


                 .
gi 447040780 241 R 241
Cdd:cd07580  252 R 252
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 6.78e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 72.24  E-value: 6.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 105 YDKRHL---FRMaDEHLHYKAGNA-RVIVEWRGWRILPLVCYDLRFPVWSRNL--NDYDLALYVANW---PApRSLHWQA 175
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARRLalDGADVLVLPAAWvrgPL-KEHHWET 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447040780 176 LLTARAIENQAYVAGcnrVGSDGNgchyR--GDSRVINPQGEIIATAdAHQATRIDAELSMAALREYREKFP 245
Cdd:NF033621 185 LLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
PLN02798 PLN02798
nitrilase
 91-245 1.22e-12

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 65.92  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  91 NRFLLVEPGGTVH-FYDKRHLF-------RMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNdYDLALYV 162
Cdd:PLN02798 105 NTHVLIDDSGEIRsSYRKIHLFdvdvpggPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFPELYQQLR-FEHGAQV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 163 ANWPAPRSL-----HWQALLTARAIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRID-AELSMAA 236
Cdd:PLN02798 184 LLVPSAFTKptgeaHWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDRLSTGIAvADIDLSL 263


                 ....*....
gi 447040780 237 LREYREKFP 245
Cdd:PLN02798 264 LDSVRTKMP 272
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-232 1.69e-10

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 60.63  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   2 PGLKITLLQ----QPLVWMdgPANLR-HFDRQLEGI-----TGRDVIVLPEmftsgfameAAASSLAQDD--VVNWMTAK 69
Cdd:COG0815  193 EPLRVALVQgnipQDLKWD--PEQRReILDRYLDLTreladDGPDLVVWPE---------TALPFLLDEDpdALARLAAA 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  70 AQQCNA-LIAGSVALQTESGSV-NRFLLVEP-GGTVHFYDKRHL------------FRMADEHL-----HYKAGNARVIV 129
Cdd:COG0815  262 AREAGApLLTGAPRRDGGGGRYyNSALLLDPdGGILGRYDKHHLvpfgeyvplrdlLRPLIPFLdlplgDFSPGTGPPVL 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 130 EWRGWRILPLVCYDLRFP--VWSRNLNDYDLALYVAN--W----PAPRSLHWQALLtaRAIENQAYVAgcnRVGSDGngc 201
Cdd:COG0815  342 DLGGVRVGPLICYESIFPelVRDAVRAGADLLVNITNdaWfgdsIGPYQHLAIARL--RAIETGRPVV---RATNTG--- 413

                        250       260       270
                 ....*....|....*....|....*....|.
gi 447040780 202 hyrgDSRVINPQGEIIATADAHQATRIDAEL 232
Cdd:COG0815  414 ----ISAVIDPDGRVLARLPLFTRGVLVAEV 440
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 4-232 1.10e-09

Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.


Pssm-ID: 143595  Cd Length: 270  Bit Score: 57.22  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQ---PLVWMDGPANLRHFDRQLEGI-----TGRDVIVLPE------MFTSGFAMEAAASSLAQDDVvnwmtak 69
Cdd:cd07571    1 LRVALVQGnipQDEKWDPEQRQATLDRYLDLTreladEKPDLVVWPEtalpfdLQRDPDALARLARAARAVGA------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  70 aqqcnALIAGSVALQTESGSV-NRFLLVEPGG-TVHFYDKRHL------------FRMADEHL-----HYKAGNARVIVE 130
Cdd:cd07571   74 -----PLLTGAPRREPGGGRYyNSALLLDPGGgILGRYDKHHLvpfgeyvplrdlLRFLGLLFdlpmgDFSPGTGPQPLL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 131 WRG-WRILPLVCYDLRFPVWSRNL--NDYDLALYVAN------WPAPRSLHWQALLtaRAIENQAYVAgcnRVGSDGngc 201
Cdd:cd07571  149 LGGgVRVGPLICYESIFPELVRDAvrQGADLLVNITNdawfgdSAGPYQHLAMARL--RAIETGRPLV---RAANTG--- 220

                        250       260       270
                 ....*....|....*....|....*....|.
gi 447040780 202 hyrgDSRVINPQGEIIATADAHQATRIDAEL 232
Cdd:cd07571  221 ----ISAVIDPDGRIVARLPLFEAGVLVAEV 247
PRK13981 PRK13981
NAD synthetase; Provisional
 34-220 1.66e-09

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 57.47  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  34 GRDVIVLPEMFTSGF-------------AMEAAASSLAQDdvvnwmTAKAQqcnALIAGSVaLQTESGSVNRFLLVEPGG 100
Cdd:PRK13981  33 GADLLLFPELFLSGYppedlllrpaflaACEAALERLAAA------TAGGP---AVLVGHP-WREGGKLYNAAALLDGGE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 101 TVHFYDKRHL-----FrmaDEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDY--DLAL------YVANWPA 167
Cdd:PRK13981 103 VLATYRKQDLpnygvF---DEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPEPAETLAEAgaELLLvpnaspYHRGKPD 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447040780 168 PRslhwQALLTARAIENQAYVAGCNRVGS------DGNgchyrgdSRVINPQGEIIATA 220
Cdd:PRK13981 180 LR----EAVLRARVRETGLPLVYLNQVGGqdelvfDGA-------SFVLNADGELAARL 227
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 4-249 3.61e-09

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 56.03  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   4 LKITLLQQplVWMDGPAnlRHFDRQLEGI-----TGRDVIVLPEMF-TSGFAME--AAASSLAQD----DVVNWMTAKAQ 71
Cdd:cd07573    1 VTVALVQM--ACSEDPE--ANLAKAEELVreaaaQGAQIVCLQELFeTPYFCQEedEDYFDLAEPpipgPTTARFQALAK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  72 QCNALIAGSVALQTESGSV-NRFLLVEPGGTVH-FYDKRHLfrmADEHLHY-----KAGNA--RVIvEWRGWRILPLVCY 142
Cdd:cd07573   77 ELGVVIPVSLFEKRGNGLYyNSAVVIDADGSLLgVYRKMHI---PDDPGYYekfyfTPGDTgfKVF-DTRYGRIGVLICW 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 143 DLRFPVWSRN--LNDYDLALY----------VANWPAPRSlHWQALLTARAIENQAYVAGCNRVG---SDGNGCHYRGDS 207
Cdd:cd07573  153 DQWFPEAARLmaLQGAEILFYptaigsepqePPEGLDQRD-AWQRVQRGHAIANGVPVAAVNRVGvegDPGSGITFYGSS 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 447040780 208 RVINPQGEIIATADAHQATRIDAELSMAALREYREKFPAWQD 249
Cdd:cd07573  232 FIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWPFFRD 273
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 2-232 6.20e-08

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 52.96  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780   2 PGLKITLLQ----QPLVWmdGPANLRH-FDRQLEGI----TGRDVIVLPEmftsgfameAAASSLAQDDVVNWMTAKAQQ 72
Cdd:PRK00302 218 PALKVALVQgnipQSLKW--DPAGLEAtLQKYLDLSrpalGPADLIIWPE---------TAIPFLLEDLPQAFLKALDDL 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  73 CN----ALIAGSVALQTESGSV---NRFLLVEPGGTVHFYDKRHL------------FR-----MADEHLHYKAGNAR-V 127
Cdd:PRK00302 287 ARekgsALITGAPRAENKQGRYdyyNSIYVLGPYGILNRYDKHHLvpfgeyvpleslLRplapfFNLPMGDFSRGPYVqP 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 128 IVEWRGWRILPLVCYDLRFP--VWSRNLNDYDLALYVAN--W----PAPrslhWQALLTA--RAIENQAYVA-GCNrvgs 196
Cdd:PRK00302 367 PLLAKGLKLAPLICYEIIFPeeVRANVRQGADLLLNISNdaWfgdsIGP----YQHFQMArmRALELGRPLIrATN---- 438

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 447040780 197 dgNGChyrgdSRVINPQGEIIATADAHQATRIDAEL 232
Cdd:PRK00302 439 --TGI-----TAVIDPLGRIIAQLPQFTEGVLDGTV 467
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 17-243 4.83e-07

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143606  Cd Length: 294  Bit Score: 49.65  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  17 DGPANLRHFDRQLEGI-----TGRDV--IVLPEMFTSGFAMEAAASSLAQD----DVVNWMTA----KAQQCNALIAGSv 81
Cdd:cd07582   18 DILANIDRINEQIDAAvgfsgPGLPVrlVVLPEYALQGFPMGEPREVWQFDkaaiDIPGPETEalgeKAKELNVYIAAN- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  82 ALQTESGSVNRFL----LVEPGGTVhFYDKRHLFRMADEHL----------HYKAGNAR-----VIVEWRGwRILPLVCY 142
Cdd:cd07582   97 AYERDPDFPGLYFntafIIDPSGEI-ILRYRKMNSLAAEGSpsphdvwdeyIEVYGYGLdalfpVADTEIG-NLGCLACE 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 143 DLRFPVWSRNL--NDYDLALY-VANWPAPRSLHWQALLTARAIENQAYVAGCNR---VGSDGNGCHYRGDSRVINPQGEI 216
Cdd:cd07582  175 EGLYPEVARGLamNGAEVLLRsSSEVPSVELDPWEIANRARALENLAYVVSANSggiYGSPYPADSFGGGSMIVDYKGRV 254

                        250       260
                 ....*....|....*....|....*...
gi 447040780 217 IATAD-AHQATRIDAELSMAALREYREK 243
Cdd:cd07582  255 LAEAGyGPGSMVAGAEIDIEALRRARAR 282
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 105-248 5.43e-07

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 49.42  E-value: 5.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 105 YDKRHLFRMAD--EHLHYKAGN-ARVIVEWRGWRILPLVCYDLRFPVWSR--NLNDYDLALYVANWPAPRSLH-WQALLT 178
Cdd:cd07568  123 YRKNHIPHVGGfwEKFYFRPGNlGYPVFDTAFGKIGVYICYDRHFPEGWRalGLNGAEIVFNPSATVAGLSEYlWKLEQP 202

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447040780 179 ARAIENQAYVAGCNRVGSD--GNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREYREKfpaWQ 248
Cdd:cd07568  203 AAAVANGYFVGAINRVGTEapWNIGEFYGSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVRDT---WQ 271
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
 132-242 1.02e-06

aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of short-chain aliphatic amides to form ammonia and the corresponding organic acid. This group includes Pseudomonas aeruginosa (Pa) AmiE, the amidase from Geobacillus pallidus RAPc8 (RAPc8 amidase), and Helicobacter pylori (Hp) AmiE and AmiF. PaAimE and HpAmiE hydrolyze various very short aliphatic amides, including propionamide, acetamide and acrylamide. HpAmiF is a formamidase which specifically hydrolyzes formamide. These proteins belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 2. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. HpAmiE , HpAmiF, and RAPc8 amidase, and PaAimE appear to be homohexameric enzymes, trimer of dimers.


Pssm-ID: 143589  Cd Length: 291  Bit Score: 48.82  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 132 RGWRILPLVCYDLRFPVWSRN--LNDYDLALYVANWPAPRSLHWQALLTARAIENQAYVAGCNRVGSDGNgCHYRGDSRV 209
Cdd:cd07565  144 KGSKIALIICHDGMYPEIAREcaYKGAELIIRIQGYMYPAKDQWIITNKANAWCNLMYTASVNLAGFDGV-FSYFGESMI 222

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447040780 210 INPQGEIIATADAHQATRIDAELSMAALREYRE 242
Cdd:cd07565  223 VNFDGRTLGEGGREPDEIVTAELSPSLVRDARK 255
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
 83-243 1.97e-06

N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.


Pssm-ID: 143593  Cd Length: 302  Bit Score: 48.07  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  83 LQTESGSVNRF---LLVEPGGTVHF-YDKRHLFRMAD-------EHL---HYKAGNarviVEWRGWRILP-----LVCYD 143
Cdd:cd07569   98 LTEDGGVKRRFntsILVDKSGKIVGkYRKVHLPGHKEpepyrpfQHLekrYFEPGD----LGFPVFRVPGgimgmCICND 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 144 LRFPVWSRNLN---------DYDLALYVANWPAP---RSLHWQALLTARAIENQAYVAGCNRVGSDgNGCHYRGDSRVIN 211
Cdd:cd07569  174 RRWPETWRVMGlqgvelvllGYNTPTHNPPAPEHdhlRLFHNLLSMQAGAYQNGTWVVAAAKAGME-DGCDLIGGSCIVA 252

                        170       180       190
                 ....*....|....*....|....*....|..
gi 447040780 212 PQGEIIATADAHQATRIDAELSMAALREYREK 243
Cdd:cd07569  253 PTGEIVAQATTLEDEVIVADCDLDLCREGRET 284
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 34-222 1.01e-05

First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143602  Cd Length: 258  Bit Score: 45.60  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  34 GRDVIVLPEMFTSGFAMEAAASSLAQDDVVNWMT-------AKAQQCnALIAGSVALQTESG-SVNRFLLVEPGGTVHFY 105
Cdd:cd07578   33 GARLIVTPEMATTGYCWYDRAEIAPFVEPIPGPTtarfaelAREHDC-YIVVGLPEVDSRSGiYYNSAVLIGPSGVIGRH 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 106 DKRHLF-----RMADEHLHYKAGNARVivewrgWRILPLVCYDLRFPVWSR--NLNDYDLALYVANW-----PAPrslHW 173
Cdd:cd07578  112 RKTHPYisepkWAADGDLGHQVFDTEI------GRIALLICMDIHFFETARllALGGADVICHISNWlaertPAP---YW 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 447040780 174 qallTARAIENQAYVAGCNRVGSDgNGCHYRGDSRVINPQGEIIATADA 222
Cdd:cd07578  183 ----INRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQASIDS 226
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 36-253 3.61e-05

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 44.00  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  36 DVIVLPEMFTSGF-------------AMEAA----ASSLAQDDVVnwmtakaqqcnaLIAGSVaLQTESGSVNRFLLVEP 98
Cdd:cd07570   34 DLVVFPELSLTGYppedlllrpdfleAAEEAleelAAATADLDIA------------VVVGLP-LRHDGKLYNAAAVLQN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780  99 GGTVHFYDKRHL-----FrmaDEHLHYKAGNARVIVEWRGWRILPLVCYDLRFP-VWSRNLNDY--DLAL------YVAN 164
Cdd:cd07570  101 GKILGVVPKQLLpnygvF---DEKRYFTPGDKPDVLFFKGLRIGVEICEDLWVPdPPSAELALAgaDLILnlsaspFHLG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 165 WPAPRslhwQALLTARAIENQAYVAGCNRVGS------DGNgchyrgdSRVINPQGEIIATADAHQATRIDAELSmaALR 238
Cdd:cd07570  178 KQDYR----RELVSSRSARTGLPYVYVNQVGGqddlvfDGG-------SFIADNDGELLAEAPRFEEDLADVDLD--RLR 244

                        250
                 ....*....|....*
gi 447040780 239 EYREKFPAWQDADEF 253
Cdd:cd07570  245 SERRRNSSFLDEEAE 259
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
 160-244 3.29e-04

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 41.32  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 160 LYVANWPAPRSLH-----WQALLTARAIENQAYVAGCNRVGS---------DGNGCHY-----RGDSRVINPQGEIIATA 220
Cdd:cd07564  176 IHVAPWPDFSPYYlsreaWLAASRHYALEGRCFVLSACQVVTeedipadceDDEEADPlevlgGGGSAIVGPDGEVLAGP 255

                         90       100
                 ....*....|....*....|....
gi 447040780 221 DAHQATRIDAELSMAALREYREKF 244
Cdd:cd07564  256 LPDEEGILYADIDLDDIVEAKLDF 279
PLN02747 PLN02747
N-carbamolyputrescine amidase
 140-249 7.69e-04

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 40.14  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447040780 140 VCYDLRFPVWSRN--LNDYDLALY---VANWPAPRSL----HWQALLTARAIENQAYVAGCNRVGSD-------GNGCHY 203
Cdd:PLN02747 155 ICWDQWFPEAARAmvLQGAEVLLYptaIGSEPQDPGLdsrdHWKRVMQGHAGANLVPLVASNRIGTEiletehgPSKITF 234

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447040780 204 RGDSRVINPQGEIIATADAHQATRIDAELSMAALREYREKFPAWQD 249
Cdd:PLN02747 235 YGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASWGVFRD 280
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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